Two recombinants of haemadin which contain RGD amino acids sequence in its forth loop was cloned, expressed and identificated on the basis of the analysis of structure and function of the haemadin and RGD sequence. The chimera genes coding for mature haemadin with inserted RGD sequence were obtained by overlapping PCR and cloned into the shuttle expression vector pPICZαA. This process was identified by restriction endonuclease digestion and DNA sequence analysis. The recombinant plasmids were electroporated into Pichia pastoris strain GS115. The recombinant proteins, HRGD1 and HRGD2, were expressed and induced by methyl alcohol, secreted into media leading by signal peptides and purificated by combination of ultrafiltration, cation exchange chromatography and gel filtration chromatography. The biological activity assays approved the chimera proteins show activity not only in antithrombin but also in antiplatete aggregation as what have been predicted.